YEAST:VPS75

Species (Taxon ID)	Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast). (559292)
Gene Name(s)	VPS75
Protein Name(s)	Vacuolar protein sorting-associated protein 75
External Links
UniProt	P53853
EMBL	Z71522 BK006947
PIR	S63214
RefSeq	NP_014153.1
PDB	2ZD7 3C9B 3C9D 3DM7 3Q33 3Q35 3Q66 3Q68
PDBsum	2ZD7 3C9B 3C9D 3DM7 3Q33 3Q35 3Q66 3Q68
ProteinModelPortal	P53853
SMR	P53853
BioGrid	35593
DIP	DIP-3896N
IntAct	P53853
MINT	MINT-544921
STRING	4932.YNL246W
MaxQB	P53853
PaxDb	P53853
PeptideAtlas	P53853
EnsemblFungi	[example_ID YNL246W]
GeneID	855475
KEGG	sce:YNL246W
CYGD	YNL246w
SGD	S000005190
eggNOG	NOG299680
HOGENOM	HOG000094457
InParanoid	P53853
OMA	PGKEFPH
OrthoDB	EOG78D7WV
BioCyc	YEAST:G3O-33243-MONOMER
EvolutionaryTrace	P53853
NextBio	979430
Proteomes	UP000002311
Genevestigator	P53853
GO	GO:0005829 GO:0005634 GO:0010698 GO:0042393 GO:0006303 GO:0006334 GO:0043085 GO:0035066 GO:0015031
InterPro	IPR002164
PANTHER	PTHR11875
Pfam	PF00956

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Extension	Notes	Status
	GO:2000617	positive regulation of histone H3-K9 acetylation	PMID:23401858^[1]	ECO:0000315			P		Figures 4, 5, and 6 describe the role of Vps75 in cryptic transcription and should be considered when analyzing Figure 7. Figure 7 shows the regulation of histone acetylation.	complete CACAO 7231
part_of	GO:0005634	nucleus	PMID:14562095^[2]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:2000617	positive regulation of histone H3-K9 acetylation	PMID:23401858^[1]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0042393	histone binding	PMID:17344218^[3]	ECO:0000353	physical interaction evidence used in manual assertion	SGD:S000000213 SGD:S000000214 SGD:S000004975 SGD:S000004976	F		Seeded From UniProt	complete
enables	GO:0042393	histone binding	PMID:17344218^[3]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0035066	positive regulation of histone acetylation	PMID:18458063^[4]	ECO:0000316	genetic interaction evidence used in manual assertion	SGD:S000003484	P		Seeded From UniProt	complete
involved_in	GO:0035066	positive regulation of histone acetylation	PMID:18458063^[4]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0035066	positive regulation of histone acetylation	PMID:18458063^[4]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0010698	acetyltransferase activator activity	PMID:19172749^[5]	ECO:0000315	mutant phenotype evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0010698	acetyltransferase activator activity	PMID:19172749^[5]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0006334	nucleosome assembly	PMID:17344218^[3]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006303	double-strand break repair via nonhomologous end joining	PMID:18036332^[6]	ECO:0000353	physical interaction evidence used in manual assertion	SGD:S000003925	P		Seeded From UniProt	complete
involved_in	GO:0006303	double-strand break repair via nonhomologous end joining	PMID:18036332^[6]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	PMID:22932476^[7]	ECO:0000314	direct assay evidence used in manual assertion		C	exists_during:(GO:0071456)	Seeded From UniProt	complete
part_of	GO:0005634	nucleus	PMID:22932476^[7]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
colocalizes_with	GO:0000785	chromatin	PMID:17344218^[3]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:21179020^[8]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P53853	F		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:19172749^[5]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P53853	F		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:19172748^[9]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P53853	F		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:18723682^[10]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P53853	F		Seeded From UniProt	complete
involved_in	GO:0043085	positive regulation of catalytic activity	GO_REF:0000108	ECO:0000364	evidence based on logical inference from manual annotation used in automatic assertion	GO:0010698	P		Seeded From UniProt	complete
involved_in	GO:0043085	positive regulation of catalytic activity	GO_REF:0000108	ECO:0000364	evidence based on logical inference from manual annotation used in automatic assertion	GO:0010698	P		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR002164	C		Seeded From UniProt	complete
involved_in	GO:0006334	nucleosome assembly	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR002164	P		Seeded From UniProt	complete
involved_in	GO:0015031	protein transport	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0653	P		Seeded From UniProt	complete
part_of	GO:0005634	nucleus	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0539 UniProtKB-SubCell:SL-0191	C		Seeded From UniProt	complete
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Notes

References

See Help:References for how to manage references in GONUTS.

↑ ^1.0 ^1.1 Xue, YM et al. (2013) Histone chaperones Nap1 and Vps75 regulate histone acetylation during transcription elongation. Mol. Cell. Biol. 33 1645-56 PubMed GONUTS page
↑ Huh, WK et al. (2003) Global analysis of protein localization in budding yeast. Nature 425 686-91 PubMed GONUTS page
↑ ^3.0 ^3.1 ^3.2 ^3.3 Selth, L & Svejstrup, JQ (2007) Vps75, a new yeast member of the NAP histone chaperone family. J. Biol. Chem. 282 12358-62 PubMed GONUTS page
↑ ^4.0 ^4.1 ^4.2 Fillingham, J et al. (2008) Chaperone control of the activity and specificity of the histone H3 acetyltransferase Rtt109. Mol. Cell. Biol. 28 4342-53 PubMed GONUTS page
↑ ^5.0 ^5.1 ^5.2 Park, YJ et al. (2008) Histone chaperone specificity in Rtt109 activation. Nat. Struct. Mol. Biol. 15 957-64 PubMed GONUTS page
↑ ^6.0 ^6.1 Jessulat, M et al. (2008) Interacting proteins Rtt109 and Vps75 affect the efficiency of non-homologous end-joining in Saccharomyces cerevisiae. Arch. Biochem. Biophys. 469 157-64 PubMed GONUTS page
↑ ^7.0 ^7.1 Dastidar, RG et al. (2012) The nuclear localization of SWI/SNF proteins is subjected to oxygen regulation. Cell Biosci 2 30 PubMed GONUTS page
↑ Lambert, JP et al. (2010) Defining the budding yeast chromatin-associated interactome. Mol. Syst. Biol. 6 448 PubMed GONUTS page
↑ Berndsen, CE et al. (2008) Molecular functions of the histone acetyltransferase chaperone complex Rtt109-Vps75. Nat. Struct. Mol. Biol. 15 948-56 PubMed GONUTS page
↑ Tang, Y et al. (2008) Structure of Vps75 and implications for histone chaperone function. Proc. Natl. Acad. Sci. U.S.A. 105 12206-11 PubMed GONUTS page

[PMID:23401858-1] 1.0 ^1.1 Xue, YM et al. (2013) Histone chaperones Nap1 and Vps75 regulate histone acetylation during transcription elongation. Mol. Cell. Biol. 33 1645-56 PubMed GONUTS page

[PMID:14562095-2] Huh, WK et al. (2003) Global analysis of protein localization in budding yeast. Nature 425 686-91 PubMed GONUTS page

[PMID:17344218-3] 3.0 ^3.1 ^3.2 ^3.3 Selth, L & Svejstrup, JQ (2007) Vps75, a new yeast member of the NAP histone chaperone family. J. Biol. Chem. 282 12358-62 PubMed GONUTS page

[PMID:18458063-4] 4.0 ^4.1 ^4.2 Fillingham, J et al. (2008) Chaperone control of the activity and specificity of the histone H3 acetyltransferase Rtt109. Mol. Cell. Biol. 28 4342-53 PubMed GONUTS page

[PMID:19172749-5] 5.0 ^5.1 ^5.2 Park, YJ et al. (2008) Histone chaperone specificity in Rtt109 activation. Nat. Struct. Mol. Biol. 15 957-64 PubMed GONUTS page

[PMID:18036332-6] 6.0 ^6.1 Jessulat, M et al. (2008) Interacting proteins Rtt109 and Vps75 affect the efficiency of non-homologous end-joining in Saccharomyces cerevisiae. Arch. Biochem. Biophys. 469 157-64 PubMed GONUTS page

[PMID:22932476-7] 7.0 ^7.1 Dastidar, RG et al. (2012) The nuclear localization of SWI/SNF proteins is subjected to oxygen regulation. Cell Biosci 2 30 PubMed GONUTS page

[PMID:21179020-8] Lambert, JP et al. (2010) Defining the budding yeast chromatin-associated interactome. Mol. Syst. Biol. 6 448 PubMed GONUTS page

[PMID:19172748-9] Berndsen, CE et al. (2008) Molecular functions of the histone acetyltransferase chaperone complex Rtt109-Vps75. Nat. Struct. Mol. Biol. 15 948-56 PubMed GONUTS page

[PMID:18723682-10] Tang, Y et al. (2008) Structure of Vps75 and implications for histone chaperone function. Proc. Natl. Acad. Sci. U.S.A. 105 12206-11 PubMed GONUTS page

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YEAST:VPS75

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